Protein Variants | Comment | Organism |
---|---|---|
additional information | mutation and complementation studies show that the uridylyltransferase activity of the bifunctional uridylyltransferase/uridylyl-removing enzyme GlnD is localized to the N-terminal region | Rhodospirillum rubrum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UTP + [protein-PII] | Rhodospirillum rubrum | GlnD plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of PII proteins, which in turn regulate a variety of other proteins. It is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity | diphosphate + uridylyl-[protein-PII] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodospirillum rubrum | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UTP + [protein-PII] | - |
Rhodospirillum rubrum | diphosphate + uridylyl-[protein-PII] | - |
? | |
UTP + [protein-PII] | GlnD plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of PII proteins, which in turn regulate a variety of other proteins. It is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity | Rhodospirillum rubrum | diphosphate + uridylyl-[protein-PII] | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GlnD | bifunctional uridylyltransferase/uridylyl-removing enzyme | Rhodospirillum rubrum |